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Protein

Heat shock protein HSP 90-alpha 1

Gene

hsp90a.1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (By similarity). Plays a key role in slow and fast muscle development in the embryo. Plays a role in myosin expression and assembly.By similarity4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei48 – 481ATPBy similarity
Binding sitei90 – 901ATPBy similarity
Binding sitei109 – 1091ATPBy similarity
Binding sitei135 – 1351ATP; via amide nitrogenBy similarity
Binding sitei393 – 3931ATPBy similarity

GO - Molecular functioni

GO - Biological processi

  • leukocyte migration Source: ZFIN
  • muscle organ development Source: UniProtKB-KW
  • myofibril assembly Source: ZFIN
  • positive regulation of nitric oxide biosynthetic process Source: UniProtKB
  • protein folding Source: InterPro
  • regulation of catalytic activity Source: GOC
  • response to metal ion Source: ZFIN
  • response to stress Source: InterPro
  • sarcomerogenesis Source: ZFIN
  • skeletal muscle myosin thick filament assembly Source: ZFIN
  • skeletal muscle thin filament assembly Source: ZFIN
  • skeletal myofibril assembly Source: ZFIN
  • striated muscle myosin thick filament assembly Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Myogenesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein HSP 90-alpha 1
Gene namesi
Name:hsp90a.1
Synonyms:hsp90, hsp90a, hsp90aa1
ORF Names:zgc:86652
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 20

Organism-specific databases

ZFINiZDB-GENE-990415-94. hsp90aa1.1.

Subcellular locationi

GO - Cellular componenti

  • A band Source: UniProtKB-SubCell
  • melanosome Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • Z disc Source: ZFIN
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941G → D in slou45; absence of thick filaments leading to loss of filamentous organization of myofibrils. 1 Publication
Mutagenesisi721 – 7255Missing : Reduced binding to unc45b. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Heat shock protein HSP 90-alpha 1PRO_0000062924Add
BLAST

Proteomic databases

PaxDbiQ90474.
PRIDEiQ90474.

Expressioni

Tissue specificityi

Strongly expressed in the early embryos within the somitic slow muscle progenitors, the adaxial cells that lie on either side of the notochord but not the notochord. Also expressed during the early differentiation of fast fibers. Detected in developing cardiac muscles and pectoral fin primordia. Not detected in mature muscle fibers.3 Publications

Developmental stagei

Barely detectable during embryogenesis at control temperatures. Distributed throughout the cytoplasm of early developing myocytes at 24 hours post fertilization (hpf).2 Publications

Inductioni

Up-regulated by heat shock in embryos and larvae with highest levels of expression in 3 day old larvae.2 Publications

Gene expression databases

BgeeiQ90474.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with unc45b and myosin.By similarity2 Publications

Protein-protein interaction databases

STRINGi7955.ENSDARP00000022302.

Structurei

3D structure databases

ProteinModelPortaliQ90474.
SMRiQ90474. Positions 7-220, 286-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi721 – 7255TPR repeat-binding

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000130044.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ90474.
KOiK04079.
OMAiTHANRIH.
OrthoDBiEOG780RM0.
PhylomeDBiQ90474.
TreeFamiTF300686.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q90474-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEKSAQPVM EEEVETFAFQ AEIAQLMSLI INTFYSNKEI FLRELISNSS
60 70 80 90 100
DALDKIRYES LTDPSKLDSC KDLKIELIPD QKERTLTIID TGIGMTKADL
110 120 130 140 150
INNLGTIAKS GTKAFMEALQ AGADISMIGQ FGVGFYSAYL VAEKVTVITK
160 170 180 190 200
HNDDEQYIWE SAAGGSFTVK PDFGESIGRG TKVILHLKED QSEYVEEKRI
210 220 230 240 250
KEVVKKHSQF IGYPITLYIE KQREKEVDLE EGEKQEEEEV AAGEDKDKPK
260 270 280 290 300
IEDLGADEDE DSKDGKNKRK KKVKEKYIDA QELNKTKPIW TRNPDDITNE
310 320 330 340 350
EYGEFYKSLS NDWEDHLAVK HFSVEGQLEF RALLFVPRRA AFDLFENKKK
360 370 380 390 400
RNNIKLYVRR VFIMDNCEEL IPEYLNFIKG VVDSEDLPLN ISREMLQQSK
410 420 430 440 450
ILKVIRKNLV KKCLDLFTEL AEDKDNYKKY YEQFSKNIKL GIHEDSQNRK
460 470 480 490 500
KLSDLLRYYT SASGDEMVSL KDYVSRMKDT QKHIYYITGE TKDQVANSAF
510 520 530 540 550
VERLRKAGLE VIYMIEPIDE YCVQQLKEYD GKNLVSVTKE GLELPEDEEE
560 570 580 590 600
KKKQDELKAK YENLCKIMKD ILDKKIEKVT VSNRLVSSPC CIVTSTYGWT
610 620 630 640 650
ANMERIMKSQ ALRDNSTMGY MTAKKHLEIN PAHPIVETLR EKAEADKNDK
660 670 680 690 700
AVKDLVILLF ETALLSSGFT LDDPQTHANR IYRMIKLGLG IDDDDSVVEE
710 720
ISQPAEEDMP VLEGDDDTSR MEEVD
Length:725
Mass (Da):83,319
Last modified:May 30, 2006 - v3
Checksum:i78CB3B97976531A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 118KSAQPVME → AHEQQMMED in AAC21567 (PubMed:10364427).Curated
Sequence conflicti217 – 2171L → F in AAH75757 (Ref. 5) Curated
Sequence conflicti300 – 3001E → D in AAH75757 (Ref. 5) Curated
Sequence conflicti447 – 4471Q → R in AAH75757 (Ref. 5) Curated
Sequence conflicti646 – 6461D → E in AAC21567 (PubMed:10364427).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068773 mRNA. Translation: AAC21567.1.
CR381646 Genomic DNA. Translation: CAI21043.1.
BC075757 mRNA. Translation: AAH75757.1.
L35586 mRNA. Translation: AAA97518.1.
PIRiJC2343.
RefSeqiNP_571403.1. NM_131328.1.
UniGeneiDr.75834.

Genome annotation databases

EnsembliENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478.
ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478.
GeneIDi30591.
KEGGidre:30591.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068773 mRNA. Translation: AAC21567.1.
CR381646 Genomic DNA. Translation: CAI21043.1.
BC075757 mRNA. Translation: AAH75757.1.
L35586 mRNA. Translation: AAA97518.1.
PIRiJC2343.
RefSeqiNP_571403.1. NM_131328.1.
UniGeneiDr.75834.

3D structure databases

ProteinModelPortaliQ90474.
SMRiQ90474. Positions 7-220, 286-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000022302.

Proteomic databases

PaxDbiQ90474.
PRIDEiQ90474.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000004756; ENSDARP00000022302; ENSDARG00000010478.
ENSDART00000170138; ENSDARP00000138112; ENSDARG00000010478.
GeneIDi30591.
KEGGidre:30591.

Organism-specific databases

CTDi30591.
ZFINiZDB-GENE-990415-94. hsp90aa1.1.

Phylogenomic databases

eggNOGiKOG0020. Eukaryota.
COG0326. LUCA.
GeneTreeiENSGT00840000130044.
HOGENOMiHOG000031988.
HOVERGENiHBG007374.
InParanoidiQ90474.
KOiK04079.
OMAiTHANRIH.
OrthoDBiEOG780RM0.
PhylomeDBiQ90474.
TreeFamiTF300686.

Miscellaneous databases

NextBioi20806959.
PROiQ90474.

Gene expression databases

BgeeiQ90474.

Family and domain databases

Gene3Di3.30.565.10. 2 hits.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of zebrafish somite development by pharmacologic inhibition of Hsp90."
    Lele Z., Hartson S.D., Martin C.C., Whitesell L., Matts R.L., Krone P.H.
    Dev. Biol. 210:56-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Embryo.
  2. "The UCS factor Steif/Unc-45b interacts with the heat shock protein Hsp90a during myofibrillogenesis."
    Etard C., Behra M., Fischer N., Hutcheson D., Geisler R., Strahle U.
    Dev. Biol. 308:133-143(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UNC45B.
  3. "Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril."
    Etard C., Roostalu U., Strahle U.
    J. Cell Biol. 180:1163-1175(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MYOSIN, SUBCELLULAR LOCATION.
    Tissue: Embryo.
  4. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  5. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  6. "HSP 90 alpha and HSP 90 beta genes are present in the zebrafish and are differentially regulated in developing embryos."
    Krone P.H., Sass J.B.
    Biochem. Biophys. Res. Commun. 204:746-752(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-135, INDUCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  7. "Specific localization of zebrafish hsp90 alpha mRNA to myoD-expressing cells suggests a role for hsp90 alpha during normal muscle development."
    Sass J.B., Weinberg E.S., Krone P.H.
    Mech. Dev. 54:195-204(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  8. "Restricted expression of the zebrafish hsp90alpha gene in slow and fast muscle fiber lineages."
    Sass J.B., Martin C.C., Krone P.H.
    Int. J. Dev. Biol. 43:835-838(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis."
    Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K., Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H., Strahle U., Wilson S.W.
    Development 135:1147-1156(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-94.
  10. "Heat-shock protein 90alpha1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos."
    Du S.J., Li H., Bian Y., Zhong Y.
    Proc. Natl. Acad. Sci. U.S.A. 105:554-559(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF 721-MET--ASP-725.

Entry informationi

Entry nameiH90A1_DANRE
AccessioniPrimary (citable) accession number: Q90474
Secondary accession number(s): Q5RG13, Q6DI33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 30, 2006
Last modified: May 11, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.